8BTY
Structure of the active form of ScpB, the C5a-peptidase from Streptococcus agalactiae.
Summary for 8BTY
| Entry DOI | 10.2210/pdb8bty/pdb |
| Descriptor | C5a peptidase, MALONIC ACID, SULFATE ION, ... (7 entities in total) |
| Functional Keywords | c5a-peptidase, virulence factor, hydrolase |
| Biological source | Streptococcus agalactiae |
| Total number of polymer chains | 2 |
| Total formula weight | 221187.66 |
| Authors | Kagawa, T.F.,Cooney, J.C.,Miclot, T.,Cullen, R. (deposition date: 2022-11-30, release date: 2023-11-15, Last modification date: 2024-02-14) |
| Primary citation | Cullen, R.,Tecza, M.,Miclot, T.,Behan, S.,Jain, M.,Avink, M.K.,Cooney, J.C.,Kagawa, T.F. The 1.7 angstrom crystal structure of the C5a peptidase from Streptococcus agalactiae (ScpB) reveals an active site competent for catalysis. Proteins, 92:427-431, 2024 Cited by PubMed Abstract: A 1.7 Å structure is presented for an active form of the virulence factor ScpB, the C5a peptidase from Streptococcus agalactiae. The previously reported structure of the ScpB active site mutant exhibited a large separation (~20 Å) between the catalytic His and Ser residues. Significant differences are observed in the catalytic domain between the current and mutant ScpB structures resulting with a high RMSD (4.6 Å). The fold of the active form of ScpB is nearly identical to ScpA (RMSD 0.2 Å), the C5a-peptidase from Streptococcus pyogenes. Both ScpA and ScpB have comparable activity against human C5a, indicating neither enzyme require host proteins for C5a-ase activity. These studies are a first step in resolving reported differences in the specificities of these enzymes. PubMed: 37921533DOI: 10.1002/prot.26625 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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